This thesis describes the design and optimization of peptide ligands of the immunoglobulin G Fc region. Peptide ligands were displayed on a bacteriophage vector in the monovalent setting. The protocols of transformation, cultivation and isolation of phagemid particles are described herein. The relative affinities of peptide ligand variants to human IgG were determined by enzyme-linked immunosorbent assay. We optimized the composition of washing, blocking and dilution buffers. We tested different phage titers, on the basis of which we determined the optimal conditions, that we used in the following tests. We also changed and optimized the original phagemid on which the peptide ligands were displayed. This way, we were able to significantly reduce the nonspecific phage adsorption, that was previously distorting the results. Finally, the peptide ligands thus obtained were compared with their parent peptide and structure-activity (affinity) relationship (SAR) analysis was performed based on the results. We were able to optimize the parent peptide, and the results can be used for further research and optimization of alternative ligands of IgG Fc region.
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